Stieglitz B I, Calvo J M
J Bacteriol. 1974 Jun;118(3):935-41. doi: 10.1128/jb.118.3.935-941.1974.
alpha-Isopropylmalate synthase and beta-isopropylmalate dehydrogenase activities were detected in extracts of the following organisms: Chromatium D, Rhodopseudomonas spheroides, Hydrogenomonas H16, Pseudomonas aeruginosa, Pseudomonas fluorescens, Vibrio extorquens, Rhizobium japonicum, Alcaligenes viscolactis, Escherichia coli B, Proteus vulgaris, Aerobacter aerogenes, Salmonella typhimurium, Micrococcus sp., Micrococcus lysodeikticus, Bacillus polymyxa, Bacillus subtilis, and Nocardia opaca. The alpha-isopropylmalate synthase activity in these extracts was inhibited by low concentrations of l-leucine. Taken together with other data, these results suggest that the isopropylmalate pathway is widespread among organisms that can synthesize leucine.
在以下生物体的提取物中检测到了α-异丙基苹果酸合酶和β-异丙基苹果酸脱氢酶的活性:嗜硫色杆菌D、球形红假单胞菌、氢单胞菌H16、铜绿假单胞菌、荧光假单胞菌、扭脱弧菌、日本根瘤菌、产碱杆菌、大肠杆菌B、普通变形杆菌、产气气杆菌、鼠伤寒沙门氏菌、微球菌属、溶壁微球菌、多粘芽孢杆菌、枯草芽孢杆菌和不透明诺卡氏菌。这些提取物中的α-异丙基苹果酸合酶活性受到低浓度L-亮氨酸的抑制。结合其他数据,这些结果表明异丙基苹果酸途径在能够合成亮氨酸的生物体中广泛存在。